6MSF
F6 APTAMER MS2 COAT PROTEIN COMPLEX
Summary for 6MSF
Entry DOI | 10.2210/pdb6msf/pdb |
Descriptor | RNA (5'-R(*CP*CP*AP*CP*AP*GP*UP*CP*AP*CP*UP*GP*GP*G)-3'), RNA (5'-R(*CP*AP*GP*UP*CP*AP*CP*UP*GP*G)-3'), PROTEIN (MS2 PROTEIN CAPSID), ... (4 entities in total) |
Functional Keywords | viral coat protein-rna complex, rna aptamer, rna stem loop, bacteriophage ms2, icosahedral virus, virus-rna complex, virus/rna |
Biological source | Enterobacterio phage MS2 |
Cellular location | Virion (Potential): P03612 |
Total number of polymer chains | 5 |
Total formula weight | 48854.06 |
Authors | Convery, M.A.,Rowsell, S.,Stonehouse, N.J.,Ellington, A.D.,Hirao, I.,Murray, J.B.,Peabody, D.S.,Phillips, S.E.V.,Stockley, P.G. (deposition date: 1998-01-06, release date: 1998-07-08, Last modification date: 2023-08-02) |
Primary citation | Convery, M.A.,Rowsell, S.,Stonehouse, N.J.,Ellington, A.D.,Hirao, I.,Murray, J.B.,Peabody, D.S.,Phillips, S.E.,Stockley, P.G. Crystal structure of an RNA aptamer-protein complex at 2.8 A resolution. Nat.Struct.Biol., 5:133-139, 1998 Cited by PubMed Abstract: The crystal structure, at 2.8 A resolution, of an RNA aptamer bound to bacteriophage MS2 coat protein has been determined. It provides an opportunity to compare the interactions of MS2 coat protein and wild type operator with those of an aptamer, whose secondary structure differs from the wild type RNA in having a three-base loop (compared to a tetraloop) and an additional base pair between this loop and the sequence-specific recognition element in the stem. The RNA binds in the same location on the coat protein as the wild type operator and maintains many of the same RNA-protein interactions. In order to achieve this, the RNA stem loop undergoes a concerted rearrangement of the 3' side while leaving the 5' side and the loop interactions largely unchanged, illustrating the ability of RNA to present similar molecular recognition surfaces from distinct primary and secondary structures. PubMed: 9461079DOI: 10.1038/nsb0298-133 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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